Dynamic Studies Through Control of Relaxation in NMR Spectroscopy

1. Front Matter

   Pages i-xix

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2. Introduction

   • Nicola Salvi

   Pages 1-7

3. Theoretical Principles

   • Nicola Salvi

   Pages 9-31

4. Analytical Models for Relaxation Dispersion Experiments

   • Nicola Salvi

   Pages 33-53

5. Experimental Methods

   • Nicola Salvi

   Pages 55-63

6. Experimental Results

   • Nicola Salvi

   Pages 65-89

7. Conclusions

   • Nicola Salvi

   Pages 91-93

8. Back Matter

   Pages 95-110

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Nicola Salvi's thesis offers a remarkably cogent view of highly sophisticated NMR methods. Salvi developed these methods in order to characterize the amplitudes and frequency ranges of local motions in biomolecules such as proteins. These local motions play an essential role since they can explain many of the remarkable properties of proteins and enable them to carry out all sorts of vital functions, from enzymatic catalysis to intermolecular recognition and signalling in cells. Salvi's work has led to numerous publications in high-impact journals.

• BioNMR
• Carr-Purcell-Meiboon-Gill (CPMG)
• Chemical Exchange
• Engrailed
• Heteronuclear Double Resonance (HDR)
• KIX
• Rotating Frame Relaxation Rates (R1ρ )
• Ubiquitin

• Department of Biological Chemistry & Molecular Pharmacology, Harvard Medical School, Boston, USA

  Nicola Salvi

Dr. Salvi completed his PhD thesis at the Swiss Federal Institute of Technology in Lausanne and he is currently a postdoctoral researcher at Harvard Medical School. He is interested in the development of Nuclear Magnetic Resonance (NMR) methods for the study of protein function and for drug discovery.

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